node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABR54121.1 | ABR55342.1 | Mevan_0211 | Mevan_1448 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.690 |
ABR54121.1 | aspS | Mevan_0211 | Mevan_0926 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | 0.746 |
ABR54121.1 | carB | Mevan_0211 | Mevan_0341 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; RimK domain protein ATP-grasp; KEGG: mmp:MMP1013 carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.445 |
ABR54121.1 | gatA | Mevan_0211 | Mevan_0822 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.846 |
ABR54121.1 | gatB | Mevan_0211 | Mevan_0243 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.859 |
ABR54121.1 | gatD | Mevan_0211 | Mevan_0579 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) amidotransferase, subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. | 0.831 |
ABR54121.1 | gatE | Mevan_0211 | Mevan_0578 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | Putative aspartyl-tRNA(Asn) amidotransferase, B subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. | 0.806 |
ABR54121.1 | pyrG | Mevan_0211 | Mevan_0028 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.493 |
ABR55342.1 | ABR54121.1 | Mevan_1448 | Mevan_0211 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | 0.690 |
ABR55342.1 | aspS | Mevan_1448 | Mevan_0926 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | 0.937 |
ABR55342.1 | carB | Mevan_1448 | Mevan_0341 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; RimK domain protein ATP-grasp; KEGG: mmp:MMP1013 carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.544 |
ABR55342.1 | gatA | Mevan_1448 | Mevan_0822 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.999 |
ABR55342.1 | gatB | Mevan_1448 | Mevan_0243 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.999 |
ABR55342.1 | gatD | Mevan_1448 | Mevan_0579 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase, subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. | 0.571 |
ABR55342.1 | gatE | Mevan_1448 | Mevan_0578 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | Putative aspartyl-tRNA(Asn) amidotransferase, B subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. | 0.558 |
ABR55342.1 | guaAA | Mevan_1448 | Mevan_0756 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | GMP synthase, small subunit; Catalyzes the synthesis of GMP from XMP. | 0.680 |
ABR55342.1 | guaAB | Mevan_1448 | Mevan_0027 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.579 |
ABR55342.1 | pyrG | Mevan_1448 | Mevan_0028 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.672 |
aspS | ABR54121.1 | Mevan_0926 | Mevan_0211 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: glutamine amidotransferase class-II; asparagine synthase; KEGG: mmp:MMP0918 asparagine synthetase (glutamine-hydrolyzing). | 0.746 |
aspS | ABR55342.1 | Mevan_0926 | Mevan_1448 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.937 |